3x0x
Crystal structure of apo-DszC from Rhodococcus erythropolis D-1
Structural highlights
FunctionDSZC1_RHOER Catalyzes the first step of the '4S' desulfurization pathway that removes covalently bound sulfur from dibenzothiophene (DBT) without breaking carbon-carbon bonds. Sulfur dioxygenase which converts DBT to DBT-sulfone (DBTO2 or DBT 5,5-dioxide) in a stepwise manner (PubMed:11229908, Ref.2). Also acts on thioxanthen-9-one and 4,6-dimethyl DBT and 2,8-dimethyl DBT (Ref.2).[1] [2] Publication Abstract from PubMedThe release of SO2 from petroleum products derived from crude oil, which contains sulfur compounds such as dibenzothiophene (DBT), leads to air pollution. The '4S' metabolic pathway catalyzes the sequential conversion of DBT to 2-hydroxybiphenyl via three enzymes encoded by the dsz operon in several bacterial species. DszC (DBT monooxygenase), from Rhodococcus erythropolis D-1 is involved in the first two steps of the '4S' pathway. Here, we determined the first crystal structure of FMN-bound DszC, and found that two distinct conformations occur in the loop region (residues 131-142) adjacent to the active site. On the basis of the DszC-FMN structure and the previously reported apo structures of DszC homologs, the binding site for DBT and DBT sulfoxide is proposed. DATABASE: The atomic coordinates and structure factors for apo-DszC (PDB code: 3X0X) and DszC-FMN (PDB code: 3X0Y) have been deposited in the Protein Data Bank (https://www.rcsb.org). Crystal structures of apo-DszC and FMN-bound DszC from Rhodococcus erythropolis D-1.,Guan LJ, Lee WC, Wang S, Ohshiro T, Izumi Y, Ohtsuka J, Tanokura M FEBS J. 2015 Jan 28. doi: 10.1111/febs.13216. PMID:25627402[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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